Thumbnail
Access Restriction
Open

Author Haerd, T. ♦ Boelens, R. ♦ Kaptein, R. ♦ Carlstedt-Duke, J. ♦ Gustafsson, J. A. ♦ Maler, B. A. ♦ Yamamoto, K. R. ♦ Hyde, E. I.
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword RADIOLOGY AND NUCLEAR MEDICINE ♦ GLUCOCORTICOIDS ♦ CROSS-LINKING ♦ RECEPTORS ♦ NUCLEAR MAGNETIC RESONANCE ♦ AMINO ACID SEQUENCE ♦ HEAVY WATER ♦ OVERHAUSER EFFECT ♦ PROTONS ♦ ZINC COMPOUNDS ♦ ADRENAL HORMONES ♦ BARYONS ♦ CHEMICAL REACTIONS ♦ CORTICOSTEROIDS ♦ ELEMENTARY PARTICLES ♦ FERMIONS ♦ HADRONS ♦ HYDROGEN COMPOUNDS ♦ HYDROXY COMPOUNDS ♦ KETONES ♦ MAGNETIC RESONANCE ♦ MEMBRANE PROTEINS ♦ MOLECULAR STRUCTURE ♦ NUCLEONS ♦ ORGANIC COMPOUNDS ♦ OXYGEN COMPOUNDS ♦ POLYMERIZATION ♦ PREGNANES ♦ PROTEINS ♦ RESONANCE ♦ STEROIDS ♦ WATER ♦ Medicine- Unsealed Radionuclides in Diagnostics
Abstract Two protein fragments containing the DNA-binding domain (DBD) of the glococorticoid receptor (GR) have been studied by two-dimensional {sup 1}H NMR spectroscopy. The two peptides (93 and 115 residues, respectively) contain a common segment corresponding to residues C440-I519 of the rat GR or residues C421-I500 of the human GR and include two Zn-binding finger domains. The structures of this segment are almost identical in the two protein fragments, as judged from chemical shifts and sequential NOE connectivities. More than 90% of all observable {sup 1}H resonances within a 71-residue segment encompassing C440-R510 (rat GR) could be sequentially assigned by standard techniques, and stereospecific assignments could be made for the methyl groups in four valine residues within this segment. Sequential NEW connectivities indicate several elements of secondary structure including two {alpha}-helical segments consisting of residues S459-E469 and P493-G504, a type I reverse turn between residues R479 and C482, a type II reverse turn between residues L475 and G478, and several regions of extended peptide conformation. No evidence for {alpha}-helical conformation was found within the two putative zinc-finger domains, indicating that the structures of these domains differ from that of TFIIIA-type zinc fingers. The authors also observe several long-range NOE connectivities within C440-R510, suggesting that the sequential assignments presented here will provide a basis for a complete structure determination of this segment of the GR.
ISSN 00062960
Educational Use Research
Learning Resource Type Article
Publisher Date 1990-09-25
Publisher Place United States
Journal Biochemistry
Volume Number 29
Issue Number 38


Open content in new tab

   Open content in new tab